Article
Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP.
Journal of molecular biology - 5 Feb 1991
Tong L A, de Vos A M, Milburn M V, Kim S H
Abstract excerpt
The biological functions of ras proteins are controlled by the bound guanine nucleotide GDP or GTP. The GTP-bound conformation is biologically active, and is rapidly deactivated to the GDP-bound conformation through interaction with GAP (GTPase Activating Protein). Most transforming mutants of ra...
Topics
- Amino Acid Sequence
- Cloning, Molecular
- Computer Simulation
- Crystallography
- GTP-Binding Proteins
- Glycine
- Guanosine Triphosphate
- Hydrogen Bonding
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Oncogene Protein p21(ras)
- Protein Conformation
- Proto-Oncogene Proteins p21(ras)
- Recombinant Proteins
- Salts
- Solubility
- Structure-Activity Relationship